Multimers of the bluetongue virus nonstructural protein, NS2, possess nucleotidyl phosphatase activity: similarities between NS2 and rotavirus NSP2.
about
Bluetongue virus RNA binding protein NS2 is a modulator of viral replication and assemblyRotavirus protein involved in genome replication and packaging exhibits a HIT-like foldPPSP: prediction of PK-specific phosphorylation site with Bayesian decision theoryMultimerization of hepatitis delta antigen is a critical determinant of RNA binding specificity.RNA-binding activity of the rotavirus phosphoprotein NSP5 includes affinity for double-stranded RNA.Rice black-streaked dwarf virus P6 self-interacts to form punctate, viroplasm-like structures in the cytoplasm and recruits viroplasm-associated protein P9-1.Two nonoverlapping domains on the Norwalk virus open reading frame 3 (ORF3) protein are involved in the formation of the phosphorylated 35K protein and in ORF3-capsid protein interactionsOncolytic bluetongue viruses: promise, progress, and perspectivesHistidine triad-like motif of the rotavirus NSP2 octamer mediates both RTPase and NTPase activitiesAn ATPase activity associated with the rotavirus phosphoprotein NSP5.Structure and assembly of the RNA binding domain of bluetongue virus non-structural protein 2.Sequence specificity in the interaction of Bluetongue virus non-structural protein 2 (NS2) with viral RNA.Phosphorylation of bluetongue virus nonstructural protein 2 is essential for formation of viral inclusion bodies.Cellular Casein Kinase 2 and Protein Phosphatase 2A Modulate Replication Site Assembly of Bluetongue Virus.Rotavirus NSP5: mapping phosphorylation sites and kinase activation and viroplasm localization domains.Mammalian reovirus nonstructural protein microNS forms large inclusions and colocalizes with reovirus microtubule-associated protein micro2 in transfected cellsHyperphosphorylation of the rotavirus NSP5 protein is independent of serine 67, [corrected] NSP2, or [corrected] the intrinsic insolubility of NSP5 is regulated by cellular phosphatases.Evidence that avian reovirus σNS is an RNA chaperone: implications for genome segment assortment.Role of the histidine triad-like motif in nucleotide hydrolysis by the rotavirus RNA-packaging protein NSP2.
P2860
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P2860
Multimers of the bluetongue virus nonstructural protein, NS2, possess nucleotidyl phosphatase activity: similarities between NS2 and rotavirus NSP2.
description
2001 nî lūn-bûn
@nan
2001 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
name
Multimers of the bluetongue vi ...... etween NS2 and rotavirus NSP2.
@ast
Multimers of the bluetongue vi ...... etween NS2 and rotavirus NSP2.
@en
type
label
Multimers of the bluetongue vi ...... etween NS2 and rotavirus NSP2.
@ast
Multimers of the bluetongue vi ...... etween NS2 and rotavirus NSP2.
@en
prefLabel
Multimers of the bluetongue vi ...... etween NS2 and rotavirus NSP2.
@ast
Multimers of the bluetongue vi ...... etween NS2 and rotavirus NSP2.
@en
P2093
P356
P1433
P1476
Multimers of the bluetongue vi ...... etween NS2 and rotavirus NSP2.
@en
P2093
Taraporewala ZF
P304
P356
10.1006/VIRO.2000.0764
P407
P577
2001-02-01T00:00:00Z